Now showing items 1-3 of 3

    • Article

      Apparent digestibility coefficient of nutrients from shrimp, mussel, diatom and seaweed by juvenile Holothuria scabra Jaeger 

      ZGA Orozco, JG Sumbing, MJH Lebata-Ramos & S Watanabe - Aquaculture Research, 2014 - Wiley
      The ability of Holothuria scabra to digest nutrients, such as organic matter (OM), protein and carbohydrate from animal and plant feed ingredients was investigated. Four test feeds prepared by mixing sand with single ingredients from animal sources (shrimp and mussel) and plant sources (diatom and seaweed) were fed to H. scabra to estimate apparent digestibility coefficient (ADC). The total assimilated nutrient (TAN) increased with ADC, whereas ingestion rate (IR) varied slightly among the feeds suggesting that ADC might be a good indicator of nutrient availability to H. scabra. The ADCOM of shrimp and mussel was significantly higher than that diatom and seaweed: 86.2%, 77.1%, 55.1% and 32.3% respectively. ADCprotein was similar for shrimp (88.7%), mussel (84.8%) and diatom (75.2%), but significantly lower in seaweed (34.4%). ADCcarbohydrate was similar in mussel (58.5%) and diatom (58.3%) as well as in seaweed (31.6) and shrimp (28.0%). ADCprotein was relatively higher than ADCcarbohydrate suggesting that H. scabra generally digests more protein than carbohydrate. Furthermore, results indicated that nutrients from animal-based feeds are more efficiently digested by H. scabra; thus, animal ingredients rich in easily digestible protein could potentially provide an efficiently balanced diet for H. scabra fed with diatom containing high easily digestible carbohydrate.
    • Article

      Molecular cloning and localization of GABAA receptor-associated protein in the rotifer Brachionus plicatilis 

      HS Marcial, K Suga, S Kinoshita, G Kaneko, A Hagiwara & S Watabe - International Review of Hydrobiology, 2014 - Wiley-VCH Verlag
      γ-Aminobutyric acid receptor type A-associated protein (GABARAP) and its homologs constitute a protein family found in many eukaryotes from yeast to human, and are known to be involved in intracellular membrane trafficking of GABAA receptors and autophagy. In this study, we cloned cDNA-encoding GABARAP from the monogonont rotifer Brachionus plicatilis and examined for its tissue distribution at the protein level in neonates, males and females. Using reverse transcription (RT)-PCR and rapid amplification of cDNA ends (RACE) techniques, we showed that like other GABARAPs, rotifer GABARAP was also composed of 117 amino acids and highly homologous to vertebrate GABARAP2 ortholog (74–76% identity). GABARAP was demonstrated with its specific antibody to be ubiquitously distributed, irrespective of neonates, males, and females, in the coronal area that covers brain and contains most mechano- and chemoreceptors. Rotifer GABARAP was also expressed in the mature eggs but not in immature eggs. Double immunostaining with mammalian anti-GABA γ receptor antibody showed that rotifer GABARAP co-localized with GABA receptor, suggesting the association of the two proteins. The presence of GABARAP in rotifer implies that it is highly conserved during evolution, and plays important roles in various biological processes.
    • Article

      Purification and properties of a non-stereospecific dehalogenase enzyme E (DehE) from Methylobacterium sp. HJ1 

      NH Jing, FH Sulaiman, RA Wahab, RV Pakingking Jr., NAA Rashid & F Huyop - African Journal of Microbiology Research, 2008 - Academic Journals
      The bacterial isolate HJ1, which was identified as a Methylobacterium sp., grew on 2, 2-dichloropropionic acid as the sole carbon source and produced a 2-haloalkanoic acid hydrolytic dehalogenase. This non-stereospecific dehalogenase E (DehE) catalysed the hydrolytic dechlorination of 2, 2-dichloropropionic acid and D, L-2-chloropropionic acid to produce pyruvate and lactate, respectively. The enzyme was purified to homogeneity and characterized. The molecular weight was 36 kDa by SDS-polyacrylamide gel electrophoresis and 72 kDa by gel filtration, suggesting that the enzyme is a protein dimer. The purified enzyme was only inhibited by HgSO4 and was non-stereospecific to haloalkanoic acids. The Km value for the hydrolysis of 2, 2-dichloropropionic acid was 0.25 mM. The enzyme removes chloride present on the α-position, but not on the β-position, of a number 2-carbon alkanoic acids.